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Post-translational modification

A monoubiquitylation pore anchor

Nature Reviews Molecular Cell Biology volume 13, page 66 (2012)Cite this article

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Dargemont and colleagues analysed a library of tagged NUPs for conjugation by ubiquitin and found that approximately half of the NUPs are targets of this modification. Although ubiquitylation was not observed on transmembrane NUPs, there was not a strong correlation between NUPs that were modified and their localization elsewhere within the NPC.

The ubiquitylation profiles observed were varied, suggesting that this modification might affect NUP functions beyond 'housekeeping' roles. To test this, the authors focused on Nup159, which resides on the cytoplasmic face of the NPC and mediates the interaction of dynein light chain 2 (Dyn2) with the NPC. They showed that Nup159 is monoubiquitylated at Lys897 by the E2 enzyme Cdc34 and the E3 ligase SCFGrr1 (Skp1–Cdc53–F box bound to the adaptor subunit Grr1) and that this modification is not important for Nup159 localization at the NPC or for Nup159 turnover. It also did not affect either nuclear transport or the overall organization of the NPC.

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ORIGINAL RESEARCH PAPER

  1. Hayakawa, A. et al. Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae. J. Cell Biol. 2 Jan 2012 doi:10.1083/jcb.201108124

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  1. Alison Schuldt
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Schuldt, A. A monoubiquitylation pore anchor. Nat Rev Mol Cell Biol 13, 66 (2012). https://doi.org/10.1038/nrm3276

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